Structural highlights
Publication Abstract from PubMedThe amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of beta-sheet-rich structures in transition from native proteins to ordered oligomers and fibres. The variation in the amino-acid sequences of the beta-structures presents a challenge to developing a model system of beta-sheets for the study of various amyloid aggregates. Here, we introduce a family of robust beta-sheet macrocycles that can serve as a platform to display a variety of heptapeptide sequences from different amyloid proteins. We have tailored these amyloid beta-sheet mimics (ABSMs) to antagonize the aggregation of various amyloid proteins, thereby reducing the toxicity of amyloid aggregates. We describe the structures and inhibitory properties of ABSMs containing amyloidogenic peptides from the amyloid-beta peptide associated with Alzheimer's disease, beta(2)-microglobulin associated with dialysis-related amyloidosis, alpha-synuclein associated with Parkinson's disease, islet amyloid polypeptide associated with type II diabetes, human and yeast prion proteins, and Tau, which forms neurofibrillary tangles. Amyloid beta-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity.,Cheng PN, Liu C, Zhao M, Eisenberg D, Nowick JS Nat Chem. 2012 Nov;4(11):927-33. doi: 10.1038/nchem.1433. Epub 2012 Sep 9. PMID:23089868[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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